How does the presence of 7-deazaguanine (7DG) affect the conformation of HsPNP?
Label:chem
Topic
The binding of 7-deazaguanine (7DG) to human purine nucleoside phosphorylase (HsPNP) may induce conformational changes in the enzyme, affecting its structure and function. Crystallographic and molecular dynamics analyses were used to investigate these changes.
From: "Crystal structure and molecular dynamics studies of human purine nucleoside phosphorylase complexed with 7-deazaguanine", Journal of Structural Biology, Volume 169, Issue 3, March 2010, Pages 379-388
Answer
The presence of 7-deazaguanine (7DG) induces conformational changes in HsPNP, particularly in regions close to the binding pocket and the loop region (Leu240–Val260). Molecular dynamics simulations show that the binding of 7DG stabilizes certain regions, such as the beta-sheet composed of residues Asn109–Leu120 and the loop formed by Ala196–Thr202, which are involved in substrate entrance and exit. Additionally, the residue Phe159, which is conserved among all PNP sequences, moves closer to the binding site when 7DG is bound, suggesting a possible "lid" mechanism for ligand specificity.
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